Q13216 (ERCC8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA excision repair protein ERCC-8

Alternative name(s):
Cockayne syndrome WD repeat protein CSA

Gene names

Name:	ERCC8
Synonyms:	CKN1, CSA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Substrate-recognition component of the CSA complex, a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, involved in transcription-coupled nucleotide excision repair. The CSA complex (DCX(ERCC8) complex) promotes the ubiquitination and subsequent proteasomal degradation of ERCC6 in a UV-dependent manner; ERCC6 degradation is essential for the recovery of RNA synthesis after transcription-coupled repair. It is required for the recruitment of XAB2, HMGN1 and TCEA1/TFIIS to a transcription-coupled repair complex which removes RNA polymerase II-blocking lesions from the transcribed strand of active genes. Ref.9 Ref.10
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Part of the CSA complex (DCX(ERCC8) complex), a DCX E3 ubiquitin-protein ligase complex containing ERCC8, RBX1, DDB1 and CUL4A; the CSA complex interacts with RNA polymerase II; upon UV irradiation it interacts with the COP9 signalosome and preferentially with the hyperphosphorylated form of RNA polymerase II. Interacts with ERCC6 and KIAA1530/UVSSA. Interacts with a subunit of RNA polymerase II TFIIH. Interacts with DDB1. Ref.8 Ref.9 Ref.12
Subcellular location	Nucleus Probable.
Involvement in disease	Cockayne syndrome A (CSA) [MIM:216400]: A rare disorder characterized by cutaneous sensitivity to sunlight, abnormal and slow growth, cachectic dwarfism, progeroid appearance, progressive pigmentary retinopathy and sensorineural deafness. There is delayed neural development and severe progressive neurologic degeneration resulting in mental retardation. Two clinical forms are recognized: in the classical form or Cockayne syndrome type 1, the symptoms are progressive and typically become apparent within the first few years or life; the less common Cockayne syndrome type 2 is characterized by more severe symptoms that manifest prenatally. Cockayne syndrome shows some overlap with certain forms of xeroderma pigmentosum. Unlike xeroderma pigmentosum, patients with Cockayne syndrome do not manifest increased freckling and other pigmentation abnormalities in the skin and have no significant increase in skin cancer. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.9 Ref.13 Ref.14 Ref.16 UV-sensitive syndrome 2 (UVSS2) [MIM:614621]: An autosomal recessive disorder characterized by cutaneous photosensitivity and mild freckling in the absence of neurological abnormalities or skin tumors. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15
Sequence similarities	Contains 5 WD repeats.

Ontologies

Keywords
Biological process	DNA damage DNA repair Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Cockayne syndrome Deafness Disease mutation Dwarfism
Domain	Repeat WD repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of DNA repair Inferred from mutant phenotype Ref.1. Source: UniProtKB proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.9. Source: UniProtKB protein autoubiquitination Inferred from direct assay Ref.8. Source: UniProtKB protein polyubiquitination Inferred from direct assay Ref.8. Source: UniProtKB response to UV Inferred from direct assay Ref.8. Source: UniProtKB response to X-ray Inferred from electronic annotation. Source: Compara response to oxidative stress Inferred from direct assay PubMed 11782547. Source: UniProtKB transcription-coupled nucleotide-excision repair Inferred from mutant phenotype Ref.10. Source: UniProtKB
Cellular_component	Cul4A-RING ubiquitin ligase complex Inferred from direct assay Ref.8. Source: UniProtKB nuclear matrix Inferred from direct assay PubMed 11782547. Source: MGI nucleoplasm Traceable author statement. Source: Reactome nucleotide-excision repair complex Inferred from direct assay Ref.8. Source: MGI
Molecular_function	protein complex binding Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERCC6	Q03468	2	EBI-596556,EBI-295284
XAB2	Q9HCS7	3	EBI-295260,EBI-295232

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13216-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q13216-2)

The sequence of this isoform differs from the canonical sequence as follows:
     185-205: HRQEILAVSWSPRYDYILATA → IFILFQTATTLSKRFNKKKRY
     206-396: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 396

396

DNA excision repair protein ERCC-8

PRO_0000050970

Regions

Repeat

41 – 72

32

WD 1

Repeat

97 – 128

32

WD 2

Repeat

184 – 215

32

WD 3

Repeat

243 – 273

31

WD 4

Repeat

332 – 362

31

WD 5

Amino acid modifications

Modified residue

390

1

Phosphoserine Ref.11

Modified residue

391

1

Phosphoserine Ref.11

Modified residue

392

1

Phosphoserine Ref.11

Natural variations

Alternative sequence

185 – 205

21

HRQEI…ILATA → IFILFQTATTLSKRFNKKKR Y in isoform 2.

VSP_013914

Alternative sequence

206 – 396

191

Missing in isoform 2.

VSP_013915

Natural variant

150

1

S → C.
Corresponds to variant rs167037 [ dbSNP | Ensembl ].

VAR_053392

Natural variant

160

1

A → T in CSA. Ref.16

VAR_063507

Natural variant

160

1

A → V in CSA. Ref.14

VAR_025380

Natural variant

194

1

W → C in CSA. Ref.16

VAR_063508

Natural variant

200

1

Y → C. Ref.4
Corresponds to variant rs4647105 [ dbSNP | Ensembl ].

VAR_016319

Natural variant

202

1

L → S in CSA. Ref.16

VAR_063509

Natural variant

205

1

A → P in CSA. Ref.13

VAR_025381

Natural variant

266

1

D → G in CSA. Ref.16

VAR_063510

Natural variant

361

1

W → C in UVSS2. Ref.15

VAR_068177

Secondary structure

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396

Helix Strand Turn

Details...

Helix

2 – 10

9

Helix

15 – 28

14

Beta strand

30 – 32

3

Beta strand

36 – 38

3

Beta strand

46 – 51

6

Turn

53 – 55

3

Beta strand

58 – 63

6

Beta strand

68 – 72

5

Beta strand

77 – 80

4

Beta strand

82 – 84

3

Beta strand

86 – 90

5

Beta strand

102 – 107

6

Beta strand

115 – 119

5

Beta strand

122 – 128

7

Turn

129 – 132

4

Beta strand

133 – 139

7

Beta strand

144 – 149

6

Beta strand

158 – 176

19

Beta strand

180 – 182

3

Beta strand

189 – 194

6

Beta strand

201 – 206

6

Beta strand

211 – 215

5

Beta strand

223 – 225

3

Turn

228 – 231

4

Turn

237 – 239

3

Beta strand

248 – 253

6

Beta strand

257 – 264

8

Beta strand

269 – 273

5

Turn

274 – 276

3

Beta strand

302 – 305

4

Beta strand

307 – 312

6

Beta strand

315 – 320

6

Turn

321 – 323

3

Beta strand

326 – 330

5

Beta strand

337 – 343

7

Turn

344 – 347

4

Beta strand

348 – 353

6

Beta strand

358 – 363

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: EC962D56226D717B	FASTA	396	44,055
	10 20 30 40 50 60 MLGFLSARQT GLEDPLRLRR AESTRRVLGL ELNKDRDVER IHGGGINTLD IEPVEGRYML 70 80 90 100 110 120 SGGSDGVIVL YDLENSSRQS YYTCKAVCSI GRDHPDVHRY SVETVQWYPH DTGMFTSSSF 130 140 150 160 170 180 DKTLKVWDTN TLQTADVFNF EETVYSHHMS PVSTKHCLVA VGTRGPKVQL CDLKSGSCSH 190 200 210 220 230 240 ILQGHRQEIL AVSWSPRYDY ILATASADSR VKLWDVRRAS GCLITLDQHN GKKSQAVESA 250 260 270 280 290 300 NTAHNGKVNG LCFTSDGLHL LTVGTDNRMR LWNSSNGENT LVNYGKVCNN SKKGLKFTVS 310 320 330 340 350 360 CGCSSEFVFV PYGSTIAVYT VYSGEQITML KGHYKTVDCC VFQSNFQELY SGSRDCNILA 370 380 390 WVPSLYEPVP DDDETTTKSQ LNPAFEDAWS SSDEEG
	Isoform 2 [UniParc]. Checksum: 6553CE607A392576	FASTA	205	23,182
	10 20 30 40 50 60 MLGFLSARQT GLEDPLRLRR AESTRRVLGL ELNKDRDVER IHGGGINTLD IEPVEGRYML 70 80 90 100 110 120 SGGSDGVIVL YDLENSSRQS YYTCKAVCSI GRDHPDVHRY SVETVQWYPH DTGMFTSSSF 130 140 150 160 170 180 DKTLKVWDTN TLQTADVFNF EETVYSHHMS PVSTKHCLVA VGTRGPKVQL CDLKSGSCSH 190 200 ILQGIFILFQ TATTLSKRFN KKKRY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Cockayne syndrome group A gene encodes a WD repeat protein that interacts with CSB protein and a subunit of RNA polymerase II TFIIH." Henning K.A., Li L., Iyer N., McDaniel L.D., Reagan M.S., Legerski R., Schultz R.A., Stefanini M., Lehmann A.R., Mayne L.V., Friedberg E.C. Cell 82:555-564(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	NIEHS SNPs program Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT CYS-200.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Uterus.
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Urinary bladder.
[8]	"The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage." Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R., Kisselev A.F., Tanaka K., Nakatani Y. Cell 113:357-367(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DDB1, IDENTIFICATION IN THE CSA COMPLEX WITH RBX1; DDB1 AND CUL4A, INTERACTION OF THE CSA COMPLEX WITH RNA POLYMERASE II AND THE COP9 SIGNALOSOME.
[9]	"CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway establishes a link between complementation factors of the Cockayne syndrome." Groisman R., Kuraoka I., Chevallier O., Gaye N., Magnaldo T., Tanaka K., Kisselev A.F., Harel-Bellan A., Nakatani Y. Genes Dev. 20:1429-1434(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ERCC6, FUNCTION AS SUBSTRATE-RECOGNITION COMPONENT OF THE CSA COMPLEX.
[10]	"Cockayne syndrome A and B proteins differentially regulate recruitment of chromatin remodeling and repair factors to stalled RNA polymerase II in vivo." Fousteri M., Vermeulen W., van Zeeland A.A., Mullenders L.H. Mol. Cell 23:471-482(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-391 AND SER-392, MASS SPECTROMETRY.
[12]	"Mutations in UVSSA cause UV-sensitive syndrome and destabilize ERCC6 in transcription-coupled DNA repair." Zhang X., Horibata K., Saijo M., Ishigami C., Ukai A., Kanno S.I., Tahara H., Neilan E.G., Honma M., Nohmi T., Yasui A., Tanaka K. Nat. Genet. 44:593-597(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH UVSSA.
[13]	"CKN1 (MIM 216400): mutations in Cockayne syndrome type A and a new common polymorphism." Cao H., Williams C., Carter M., Hegele R.A. J. Hum. Genet. 49:61-63(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CSA PRO-205.
[14]	"Characterisation of novel mutations in Cockayne syndrome type A and xeroderma pigmentosum group C subjects." Ridley A.J., Colley J., Wynford-Thomas D., Jones C.J. J. Hum. Genet. 50:151-154(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CSA VAL-160.
[15]	"A UV-sensitive syndrome patient with a specific CSA mutation reveals separable roles for CSA in response to UV and oxidative DNA damage." Nardo T., Oneda R., Spivak G., Vaz B., Mortier L., Thomas P., Orioli D., Laugel V., Stary A., Hanawalt P.C., Sarasin A., Stefanini M. Proc. Natl. Acad. Sci. U.S.A. 106:6209-6214(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT UVSS2 CYS-361.
[16]	"Mutation update for the CSB/ERCC6 and CSA/ERCC8 genes involved in Cockayne syndrome." Laugel V., Dalloz C., Durand M., Sauvanaud F., Kristensen U., Vincent M.C., Pasquier L., Odent S., Cormier-Daire V., Gener B., Tobias E.S., Tolmie J.L., Martin-Coignard D., Drouin-Garraud V., Heron D., Journel H., Raffo E., Vigneron J. , Lyonnet S., Murday V., Gubser-Mercati D., Funalot B., Brueton L., Sanchez Del Pozo J., Munoz E., Gennery A.R., Salih M., Noruzinia M., Prescott K., Ramos L., Stark Z., Fieggen K., Chabrol B., Sarda P., Edery P., Bloch-Zupan A., Fawcett H., Pham D., Egly J.M., Lehmann A.R., Sarasin A., Dollfus H. Hum. Mutat. 31:113-126(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CSA THR-160; CYS-194; SER-202 AND GLY-266.
+	Additional computationally mapped references.

Web resources

Allelic variations of the XP genes

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

NIEHS-SNPs

Mendelian genes excision repair cross-complementing rodent repair deficiency, complementation group 8 (ERCC8)

Leiden Open Variation Database (LOVD)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U28413 mRNA. Translation: AAA82605.1.
CR536563 mRNA. Translation: CAG38800.1.
BT020021 mRNA. Translation: AAV38824.1.
AY213194 Genomic DNA. Translation: AAO21128.1.
AK314511 mRNA. Translation: BAG37111.1.
CH471123 Genomic DNA. Translation: EAW55004.1.
BC009793 mRNA. Translation: AAH09793.1.

IPI

IPI00012284.
IPI00386696.

PIR

A57090.

RefSeq

NP_000073.1. NM_000082.3.

UniGene

Hs.435237.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4A11	X-ray	3.31	B	1-396	[»]

ProteinModelPortal

Q13216.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-291N.

IntAct

Q13216. 8 interactions.

MINT

MINT-1417899.

STRING

9606.ENSP00000265038.

PTM databases

PhosphoSite

Q13216.

Polymorphism databases

DMDM

3121917.

Proteomic databases

PaxDb

Q13216.

PRIDE

Q13216.

Protocols and materials databases

DNASU

1161.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265038; ENSP00000265038; ENSG00000049167.

GeneID

1161.

KEGG

hsa:1161.

UCSC

uc003jsl.3. human.
uc003jsn.3. human.

Organism-specific databases

CTD

1161.

GeneCards

GC05M060169.

H-InvDB

HIX0004887.

HGNC

HGNC:3439. ERCC8.

MIM

216400. phenotype.
609412. gene.
614621. phenotype.

neXtProt

NX_Q13216.

Orphanet

90321. Cockayne syndrome type 1.
90322. Cockayne syndrome type 2.
90324. Cockayne syndrome type 3.
178338. UV-sensitive syndrome.

PharmGKB

PA27853.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2319.

HOGENOM

HOG000248233.

HOVERGEN

HBG005409.

InParanoid

Q13216.

KO

K10570.

OMA

TMLRGHY.

OrthoDB

EOG4SN1NR.

PhylomeDB

Q13216.

Enzyme and pathway databases

Reactome

REACT_216. DNA Repair.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q13216.

Bgee

Q13216.

CleanEx

HS_ERCC8.

Genevestigator

Q13216.

GermOnline

ENSG00000049167. Homo sapiens.

Family and domain databases

Gene3D

2.130.10.10. 1 hit.

InterPro

IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]

Pfam

PF00400. WD40. 5 hits.
[Graphical view]

PRINTS

PR00320. GPROTEINBRPT.

SMART

SM00320. WD40. 5 hits.
[Graphical view]

SUPFAM

SSF50978. WD40_like. 1 hit.

PROSITE

PS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

1161.

NextBio

4822.

SOURCE

Search...

Entry information

Entry name

ERCC8_HUMAN

Accession

Primary (citable) accession number: Q13216
Secondary accession number(s): B2RB64, Q6FHX5, Q96GB9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 130 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.